Journal article

Characterization of a Listeria monocytogenes Protein Interfering with Rab5a

Alvarez-Dominguez C, Madrazo-Toca F, Fernandez-Prieto L, Vandekerckhove J, Pareja E, Tobes R, Gomez-Lopez M, Del Cerro-Vadillo E, Fresno M, Leyva-Cobián F, Carrasco-Marín E ...see all

Traffic, vol. 9, issue 3 (2008) pp. 325-337

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Listeria monocytogenes (LM) phagocytic strategy implies recruitment and inhibition of Rab5a. Here, we identify a Listeria protein that binds to Rab5a and is responsible for Rab5a recruitment to phagosomes and impairment of the GDP/GTP exchange activity. This protein was identified as a glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Listeria (p40 protein, Lmo 2459). The p40 protein was found within the phagosomal membrane. Analysis of the sequence of LM p40 protein revealed two enzymatic domains: the nicotinamide adenine dinucleotide (NAD)-binding domain at the N-terminal and the C-terminal glycolytic domain. The putative ADP-ribosylating ability of this Listeria protein located in the N-terminal domain was examined and showed some similarities to the activity and Rab5a inhibition exerted by Pseudomonas aeruginosa ExoS onto endosome-endosome fusion. Listeria p40 caused Rab5a-specific ADP ribosylation and blocked Rab5a-exchange factor (Vps9) and GDI interaction and function, explaining the inhibition observed in Rab5a-mediated phagosome-endosome fusion. Meanwhile, ExoS impaired Rab5-early endosomal antigen 1 (EEA1) interaction and showed a wider Rab specificity. Listeria GAPDH might be the first intracellular gram-positive enzyme targeted to Rab proteins with ADP-ribosylating ability and a putative novel virulence factor.

Author-supplied keywords

  • ADP-ribosylation
  • GDP/GTP exchange
  • Glyceraldehyde-3-phosphate dehydrogenase
  • Listeria
  • Phagocytosis
  • Rab5a

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  • carmen alvarez-dominguezInstituto de Investigación Marqués de Valdecilla, IDIVAL

  • Fidel Madrazo-Toca

  • Lorena Fernandez-Prieto

  • Joël Vandekerckhove

  • Eduardo Pareja

  • Raquel Tobes

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